Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly.

Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Research Abstract Details 

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Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Abstract Text:

N Yadava,P Potluri,I E Scheffler,

There have been several reports on the phosphorylation of various subunits of NADH-ubiquinone oxidoreductase (complex I) in mammalian mitochondria. The effects of phosphorylation on assembly or activity of these subunits have not been investigated directly. The cAMP-dependent phosphorylation of the MWFE and ESSS subunits in isolated bovine heart mitochondria has been recently reported. We have investigated the significance of potential phosphorylation of these two subunits in complex I assembly and function by mutational analysis of the phosphorylation sites. Chinese hamster mutant cell lines missing either the MWFE or the ESSS subunits were transfected and complemented with the corresponding wild type and mutant cDNAs made by site-directed mutagenesis. In MWFE the serine 55 was substituted by alanine, glutamate, glutamine, and aspartate (S55A, S55E, S55Q, and S55D, respectively). The glutamate substitutions might be expected to mimic the phosphorylated state of the protein. With the exception of the MWFE(S55A) mutant protein the assembly of complex I was completely blocked, and no activity could be detected. Various substitutions in the ESSS protein (S2A, S2E, S8A, S8E, T21A, T21E, S30A, S30E) appeared to cause lower levels of mature protein and a significantly reduced complex I activity measured polarographically. The ESSS (S2/8A) double mutant protein caused a complete failure to assemble. These mutational analyses suggest that if phosphorylation occurs in vivo, the effects on complex I activity are significant.

Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Publishing Authors By Initials

N Yadava,P Potluri,IE Scheffler,

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Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The international journal of biochemistry & cell b

VOLUME: 40

Page Numbers: 447-60

Journal Abbreviation: Int. J. Biochem. Cell Biol.

ISSN: 1357-2725

DAY: 6

MONTH: 09

YEAR: 2007

Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Information

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LANGUAGE: eng

NlmUniqueID: 9508482

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AFFILIATION: Buck Institute for Age Research, Novato, CA 94945, United States.

Country: England

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MEDLINETA: Int J Biochem Cell Biol

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